Crystallization and preliminary X-ray diffraction analysis of the N-terminal domain of human coronavirus OC43 nucleocapsid protein

I. Jung Chen, Chia Cheng Chou, Chia Ling Liu, Cheng Chung Lee, Lou Sing Kan, Ming Hon Hou

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)

Abstract

The N-terminal domain of nucleocapsid protein from human coronavirus OC43 (HCoV-OC43 N-NTD) mostly contains positively charged residues and has been identified as being responsible for RNA binding during ribonucleocapsid formation in the coronavirus. In this study, the crystallization and preliminary crystallographic analysis of HCoV-OC43 N-NTD (amino acids 58-195) with a molecular weight of 20 kDa are reported. HCoV-OC43 N-NTD was crystallized at 293 K using PEG 1500 as a precipitant and a 99.9% complete native data set was collected to 1.7 Å resolution at 100 K with an overall Rmerge of 5.0%. The crystals belonged to the hexagonal space group P65, with unit-cell parameters a = 81.57, c = 42.87 Å. Solvent-content calculations suggest that there is likely to be one subunit of N-NTD in the asymmetric unit.

Original languageEnglish
Pages (from-to)815-818
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume66
Issue number7
DOIs
Publication statusPublished - 2010
Externally publishedYes

Keywords

  • human coronavirus OC43
  • N-terminal domain
  • nucleocapsid proteins
  • RNA binding

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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